NDLI: High-resolution solid-state 13C NMR of the LH1 from Rhodospirillum rubrum

Content Provider	Springer Nature Link
Author	Yoza, Kenji Wang, Zheng Yu Kobayashi, Masayuki zawa, Tsuneri
Copyright Year	1997
Abstract	High-resolution solid-state 13C NMR spectra of the light-harvesting antenna complex (LH1) from Rhodospirillum rubrum were observed for the first time by cross-polarization (CP), magic angle spinning (MAS) methods with a total elimination of spinning side band technique (TOSS). Chemical shift analysis of the CP/MAS/TOSS 13C NMR spectra confirmed that the LH1 consists mainly of α-helices in the solid state. Time constants of cross polarization (TCH) and relaxation time T1 in a rotating frame (T1ρH) were determined from the experiments at various contact times. Smaller values of TCH were obtained for the carbons attached directly with protons in a rigid state. Relaxation times T1ρH revealed the dynamic structure of the complex and showed that bacteriochlorophyll a in the LH1 has high internal mobility even in the solid state. The proton spin-lattice relaxation time in a laboratory frame (T1H) determined by the 13C NMR signal amplitude changes suggested that protons in the LH1 proteins have such strong interaction among them that the spins of all protons in the protein can diffuse through spin-lattice-relaxation.
Starting Page	167
Ending Page	173
Page Count	7
File Format	PDF
ISSN	01668595
Journal	Photosynthesis Research
Volume Number	52
Issue Number	2
e-ISSN	15735079
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1997-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Plant Physiology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine Biochemistry

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